Lactase is an enzyme produced by many organisms and is essential to the complete digestion of whole milk. It breaks down the sugar lactose into its component parts, galactose and glucose. Lactase is found in the brush border of the small intestine of humans and other mammals. People deficient in lactase or lacking functional lactase may experience the symptoms of lactose intolerance after consuming milk products. Microbial β-galactosidase can be purchased as a food supplement and is added to milk to produce "lactose-free" milk products.
β-Galactosidase is a glycoside hydrolase enzyme that catalyzes hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides.
Mannans are polymers containing the sugar mannose as a principal component. They are a type of polysaccharide found in hemicellulose, a major source of biomass found in higher plants such as softwoods. These polymers also typically contain two other sugars, galactose and glucose. They are often branched.
A glycosidic bond or glycosidic linkage is a type of ether bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate.
Maltose, also known as maltobiose or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) bond. In the isomer isomaltose, the two glucose molecules are joined with an α(1→6) bond. Maltose is the two-unit member of the amylose homologous series, the key structural motif of starch. When beta-amylase breaks down starch, it removes two glucose units at a time, producing maltose. An example of this reaction is found in germinating seeds, which is why it was named after malt. Unlike sucrose, it is a reducing sugar.
The lactose operon is an operon required for the transport and metabolism of lactose in E. coli and many other enteric bacteria. Although glucose is the preferred carbon source for most enteric bacteria, the lac operon allows for the effective digestion of lactose when glucose is not available through the activity of β-galactosidase. Gene regulation of the lac operon was the first genetic regulatory mechanism to be understood clearly, so it has become a foremost example of prokaryotic gene regulation. It is often discussed in introductory molecular and cellular biology classes for this reason. This lactose metabolism system was used by François Jacob and Jacques Monod to determine how a biological cell knows which enzyme to synthesize. Their work on the lac operon won them the Nobel Prize in Physiology in 1965.
In chemistry, a glycoside is a molecule in which a sugar is bound to another functional group via a glycosidic bond. Glycosides play numerous important roles in living organisms. Many plants store chemicals in the form of inactive glycosides. These can be activated by enzyme hydrolysis, which causes the sugar part to be broken off, making the chemical available for use. Many such plant glycosides are used as medications. Several species of Heliconius butterfly are capable of incorporating these plant compounds as a form of chemical defense against predators. In animals and humans, poisons are often bound to sugar molecules as part of their elimination from the body.
β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. Alternative names for β-fructofuranosidase EC 3.2.1.26 include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase. The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertase is a glycoprotein that hydrolyses (cleaves) the non-reducing terminal β-fructofuranoside residues. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. Invertase cleaves the α-1,2-glycosidic bond of sucrose.
Raffinose is a trisaccharide composed of galactose, glucose, and fructose. It can be found in beans, cabbage, brussels sprouts, broccoli, asparagus, other vegetables, and whole grains. Raffinose can be hydrolyzed to D-galactose and sucrose by the enzyme α-galactosidase (α-GAL), an enzyme synthesized by bacteria found in the large intestine. α-GAL also hydrolyzes other α-galactosides such as stachyose, verbascose, and galactinol, if present. In plants, raffinose plays a significant role in stress responses, particularly temperature sensitivity, seed vigour, resistance to pathogens, and desiccation.
α-Galactosidase is a glycoside hydrolase enzyme that catalyses the following reaction:
ortho-Nitrophenyl-β-galactoside (ONPG) is a colorimetric and spectrophotometric substrate for detection of β-galactosidase activity. This compound is normally colorless. However, if β-galactosidase is present, it hydrolyzes the ONPG molecule into galactose and ortho-nitrophenol. The latter compound has a yellow color that can be used to check for enzyme activity by means of a colorimetric assay. β-Galactosidase is required for lactose utilization, so the intensity of the color produced can be used as a measure of the enzymatic rate.
X-gal is an organic compound consisting of galactose linked to a substituted indole. The compound was synthesized by Jerome Horwitz and collaborators in 1964. The formal chemical name is often shortened to less accurate but also less cumbersome phrases such as bromochloroindoxyl galactoside. The X from indoxyl may be the source of the X in the X-gal contraction. X-gal is often used in molecular biology to test for the presence of an enzyme, β-galactosidase, in the place of its usual target, a β-galactoside. It is also used to detect activity of this enzyme in histochemistry and bacteriology. X-gal is one of many indoxyl glycosides and esters that yield insoluble blue compounds similar to indigo dye as a result of enzyme-catalyzed hydrolysis.
Galactosidases are enzymes that catalyze the hydrolysis of galactosides into monosaccharides.
The term glycosynthase refers to a class of proteins that have been engineered to catalyze the formation of a glycosidic bond. Glycosynthase are derived from glycosidase enzymes, which catalyze the hydrolysis of glycosidic bonds. They were traditionally formed from retaining glycosidase by mutating the active site nucleophilic amino acid to a small non-nucleophilic amino acid. More modern approaches use directed evolution to screen for amino acid substitutions that enhance glycosynthase activity.
The enzyme 6-phospho-β-galactosidase (EC 3.2.1.85) catalyzes the following reaction:
Molecular imaging is broadly defined as the visualization of molecular and cellular processes on either a macro- or microscopic level. Because of its high spatial resolution and ability to noninvasively visualize internal organs, magnetic resonance (MR) imaging is widely believed to be an ideal platform for in vivo molecular imaging. For this reason, MR contrast agents that can detect molecular events are an active field of research. One group of compounds that has shown particular promise is enzyme-activated MR contrast agents.
Oligosaccharides and polysaccharides are an important class of polymeric carbohydrates found in virtually all living entities. Their structural features make their nomenclature challenging and their roles in living systems make their nomenclature important.
Carbohydrate synthesis is a sub-field of organic chemistry concerned with generating complex carbohydrate structures from simple units (monosaccharides). The generation of carbohydrate structures usually involves linking monosaccharides or oligosaccharides through glycosidic bonds, a process called glycosylation. Therefore, it is important to construct glycosidic linkages that have optimum molecular geometry (stereoselectivity) and the stable bond (regioselectivity) at the reaction site.
Galactosidase alpha is an enzyme that in humans is encoded by the GLA gene.
Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds. Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. Many types of glucanases share similar amino acid sequences but vastly different substrates. Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active.
